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Related Concept Videos

Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
Ion Channels01:19

Ion Channels

The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
Ion channels are specialized integral membrane proteins on the plasma membrane that allow specific...
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...

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Related Experiment Video

Updated: Jul 8, 2026

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers
09:54

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers

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Mechanosensitive membrane channels in action.

Serge Yefimov1, Erik van der Giessen, Patrick R Onck

  • 1Zernike Institute for Advanced Materials, Department of Applied Physics, University of Groningen, Nijenborgh, Groningen, The Netherlands.

Biophysical Journal
|January 15, 2008
PubMed
Summary
This summary is machine-generated.

Molecular dynamics simulations reveal how Mycobacterium tuberculosis MscL channels open in response to membrane tension. A novel peptide model shows both wild-type and V21D mutant channels expand like an iris to conduct ions.

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Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers
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Single-Molecule Imaging of Lateral Mobility and Ion Channel Activity in Lipid Bilayers using Total Internal Reflection Fluorescence (TIRF) Microscopy
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Single-Molecule Imaging of Lateral Mobility and Ion Channel Activity in Lipid Bilayers using Total Internal Reflection Fluorescence (TIRF) Microscopy

Published on: February 17, 2023

Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • Mechanosensitive channels (MSCs) are crucial for cellular adaptation to mechanical stress.
  • Mycobacterium tuberculosis MscL (Tb-MscL) is a well-studied bacterial MSC involved in osmotic homeostasis.
  • Understanding the gating mechanism of Tb-MscL provides insights into mechanotransduction.

Purpose of the Study:

  • To investigate the tension-driven gating mechanism of Tb-MscL at near-atomic detail.
  • To characterize the conformational changes of both wild-type and V21D mutant Tb-MscL under simulated hypoosmotic shock.
  • To apply a novel coarse-grained peptide model for accurate simulation of membrane protein dynamics.

Main Methods:

  • Coarse-grained molecular dynamics simulations using a novel thermodynamic peptide model.
  • Simulations of Tb-MscL (wild-type and V21D mutant) embedded in a lipid bilayer.
  • Application of increasing membrane tension to mimic hypoosmotic stress up to the bilayer rupture threshold.

Main Results:

  • Both wild-type and V21D Tb-MscL channels undergo significant conformational changes, exhibiting an iris-like expansion.
  • Channel opening to a conducting state occurs on the microsecond timescale.
  • The V21D mutant shows more pronounced pore expansion, correlating with its known gain-of-function phenotype.

Conclusions:

  • Tb-MscL gating is driven by membrane tension and proceeds via an iris-like expansion mechanism.
  • The V21D mutation enhances channel opening, consistent with experimental observations.
  • Coarse-grained simulations with advanced peptide models are effective for studying mechanosensitive channel dynamics.